1ffh
From Proteopedia
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| - | [[Image:1ffh.gif|left|200px]]<br /> | + | [[Image:1ffh.gif|left|200px]]<br /><applet load="1ffh" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1ffh" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="1ffh, resolution 2.05Å" /> | caption="1ffh, resolution 2.05Å" /> | ||
'''N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS'''<br /> | '''N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. | + | 1FFH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_aquaticus Thermus aquaticus] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Known structural/functional Sites: <scene name='pdbsite=I:Gtpase Binding Site Identified By Conserved Motifs I-Iv'>I</scene>, <scene name='pdbsite=II:Gtpase Binding Site Identified By Conserved Motifs I-Iv'>II</scene>, <scene name='pdbsite=III:Gtpase Binding Site Identified By Conserved Motifs I-Iv'>III</scene> and <scene name='pdbsite=IV:Gtpase Binding Site Identified By Conserved Motifs I-Iv'>IV</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FFH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: srp]] | [[Category: srp]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 15:15:45 2007'' |
Revision as of 13:05, 18 December 2007
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N AND GTPASE DOMAINS OF THE SIGNAL SEQUENCE RECOGNITION PROTEIN FFH FROM THERMUS AQUATICUS
Overview
The signal-recognition particle (SRP) and its receptor (SR) function in, the co-translational targeting of nascent protein-ribosome complexes to, the membrane translocation apparatus. The SRP protein subunit (termed Ffh, in bacteria) that recognizes the signal sequence of nascent polypeptides, is a GTPase, as is the SR-alpha subunit (termed FtsY). Ffh and FtsY, interact directly, each stimulating the GTP hydrolysis activity of the, other. The sequence of Ffh suggests three domains: an amino-terminal N, domain of unknown function, a central GTPase G domain, and a, methionine-rich M domain that binds both SRP RNA and signal peptides., Sequence conservation suggests that structurally similar N and G domains, are present in FtsY. Here we report the structure of the nucleotide-free, form of the NG fragment of Ffh. Consistent with a role for apo Ffh in, protein targeting, the side chains of the empty active-site pocket form a, tight network of interactions which may stabilize the nucleotide-free, protein. The structural relationship between the two domains suggests that, the N domain senses or controls the nucleotide occupancy of the GTPase, domain. A structural subdomain unique to these evolutionarily conserved, GTPases constitutes them as a distinct subfamily in the GTPase, superfamily.
About this Structure
1FFH is a Single protein structure of sequence from Thermus aquaticus with MG as ligand. Known structural/functional Sites: , , and . Full crystallographic information is available from OCA.
Reference
Structure of the conserved GTPase domain of the signal recognition particle., Freymann DM, Keenan RJ, Stroud RM, Walter P, Nature. 1997 Jan 23;385(6614):361-4. PMID:9002524
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